ID SDHB_XENLA Reviewed; 282 AA. AC Q3B8J8; Q7ZYB6; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 88. DE RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial; DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P21912}; DE AltName: Full=Iron-sulfur subunit of complex II; DE Short=Ip; DE Flags: Precursor; GN Name=sdhb; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo, and Testis; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Iron-sulfur protein (IP) subunit of succinate dehydrogenase CC (SDH) that is involved in complex II of the mitochondrial electron CC transport chain and is responsible for transferring electrons from CC succinate to ubiquinone (coenzyme Q). {ECO:0000250|UniProtKB:P21912}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + succinate = a quinol + fumarate; CC Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806, CC ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1; CC Evidence={ECO:0000250|UniProtKB:P21912}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000250|UniProtKB:Q007T0}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:Q007T0}; CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; CC Evidence={ECO:0000250|UniProtKB:Q007T0}; CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:Q007T0}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:Q007T0}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q007T0}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate CC from succinate (eukaryal route): step 1/1. CC -!- SUBUNIT: Component of complex II composed of four subunits: the CC flavoprotein (FP) sdha, iron-sulfur protein (IP) sdhb, and a cytochrome CC b composed of sdhc and sdhd. {ECO:0000250|UniProtKB:P21912}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:Q9YHT2}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q9YHT2}; Matrix side CC {ECO:0000250|UniProtKB:Q9YHT2}. CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase CC iron-sulfur protein family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC043859; AAH43859.1; -; mRNA. DR EMBL; BC106300; AAI06301.1; -; mRNA. DR RefSeq; NP_001080247.1; NM_001086778.1. DR AlphaFoldDB; Q3B8J8; -. DR SMR; Q3B8J8; -. DR BioGRID; 98181; 2. DR DNASU; 379939; -. DR GeneID; 379939; -. DR KEGG; xla:379939; -. DR AGR; Xenbase:XB-GENE-970197; -. DR CTD; 379939; -. DR Xenbase; XB-GENE-970197; sdhb.S. DR OrthoDB; 119960at2759; -. DR UniPathway; UPA00223; UER01006. DR Proteomes; UP000186698; Chromosome 7S. DR Bgee; 379939; Expressed in testis and 19 other cell types or tissues. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB. DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB. DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; ISS:UniProtKB. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:UniProtKB. DR GO; GO:0048039; F:ubiquinone binding; ISS:UniProtKB. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR CDD; cd00207; fer2; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1. DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR012675; Beta-grasp_dom_sf. DR InterPro; IPR009051; Helical_ferredxn. DR InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S. DR InterPro; IPR025192; Succ_DH/fum_Rdtase_N. DR NCBIfam; TIGR00384; dhsB; 1. DR PANTHER; PTHR11921:SF29; SUCCINATE DEHYDROGENASE [UBIQUINONE] IRON-SULFUR SUBUNIT, MITOCHONDRIAL; 1. DR PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 1. DR Pfam; PF13085; Fer2_3; 1. DR Pfam; PF13534; Fer4_17; 1. DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 1. PE 2: Evidence at transcript level; KW 2Fe-2S; 3Fe-4S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; KW Reference proteome; Transit peptide; Transport; Tricarboxylic acid cycle. FT TRANSIT 1..26 FT /note="Mitochondrion" FT /evidence="ECO:0000250|UniProtKB:P21912" FT CHAIN 27..282 FT /note="Succinate dehydrogenase [ubiquinone] iron-sulfur FT subunit, mitochondrial" FT /id="PRO_0000343802" FT DOMAIN 42..135 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT DOMAIN 178..208 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 95 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 100 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 103 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 115 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 188 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 191 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 194 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 198 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 203 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT /ligand_note="ligand shared with dhsd" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 245 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 251 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 255 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT CONFLICT 164 FT /note="K -> E (in Ref. 1; AAH43859)" FT /evidence="ECO:0000305" FT CONFLICT 279 FT /note="A -> V (in Ref. 1; AAH43859)" FT /evidence="ECO:0000305" SQ SEQUENCE 282 AA; 31777 MW; FCEE9AA00E84E689 CRC64; MAAVVFSLRR SGPVLRLSGA LQVSRGAQTA AAPASQAAAR IKKFAIYRWD PDKPGDKPRM QTYEVDLNTC GPMVLDALIK IKNEVDPTLT FRRSCREGIC GSCAMNINGG NTLACTVRID TNLSKVSKIY PLPHMYVVKD LVPDLSNFYA QYKSIEPYLK KKDKSQQGKE QYLQSIEDRD KLDGLYECIL CACCSTSCPS YWWNADKYLG PAVLMQAYRW MIDSRDDFTE ERLSKLQDPF SLYRCHTIMN CTRTCPKGLN PGKAIAEIKK MMAMYKERAV SA //